1.14.13.122: chlorophyllide-a oxygenase
This is an abbreviated version!
For detailed information about chlorophyllide-a oxygenase, go to the full flat file.
Word Map on EC 1.14.13.122
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1.14.13.122
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light-harvesting
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antenna
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photosystems
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protochlorophyllide
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rieske
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7-hydroxymethyl
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b-less
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prochlorophytes
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dark-induced
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chelatase
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pheophorbide
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lhcii
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high-light
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acaryochloris
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magnesium-protoporphyrin
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low-light
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hollandica
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prochlorothrix
- 1.14.13.122
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light-harvesting
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antenna
-
photosystems
- protochlorophyllide
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rieske
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7-hydroxymethyl
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b-less
- prochlorophytes
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dark-induced
- chelatase
- pheophorbide
- lhcii
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high-light
- acaryochloris
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magnesium-protoporphyrin
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low-light
- hollandica
- prochlorothrix
Reaction
Synonyms
AtPTC52, CAO, CAO1, Cao2, CAO_1, chlorophyll a oxygenase, chlorophyll a oxygenase 1, chlorophyll a oxygenase/chlorophyll b synthase, chlorophyllide a oxygenase, chlorophyllide a oxygenase 1, EC 1.13.12.14, fch2, OsCAO1, Pchlide a oxygenase, PGL, protochlorophyllide a oxygenase, ZmCAO1
ECTree
1.14.13.122 chlorophyllide-a oxygenaseAdvanced search results
results (
results (Engineering
Engineering on EC 1.14.13.122 - chlorophyllide-a oxygenase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
A247D
C127A
22% drop in protochlorophyllide a-oxygenase activity in the generated mutant proteins relative to the wild-type activity
C147A
36.4% drop in protochlorophyllide a-oxygenase activity in the generated mutant proteins relative to the wild-type activity
E136V
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amino acid mutation within A-domain, increased stability of the fusion enzyme, K157R alone without stability effect, deletions from Q97 up to or beyond H106 result in stability signal equivalent to a lack of the entire A-domain
F286A
0.5% drop in protochlorophyllide a-oxygenase activity in the generated mutant proteins relative to the wild-type activity
F337A
20% drop in protochlorophyllide a-oxygenase activity in the generated mutant proteins relative to the wild-type activity
F417A
0% drop in protochlorophyllide a-oxygenase activity in the generated mutant proteins relative to the wild-type activity
H129A
25.5% drop in protochlorophyllide a-oxygenase activity in the generated mutant proteins relative to the wild-type activity
H150A
24.5% drop in protochlorophyllide a-oxygenase activity in the generated mutant proteins relative to the wild-type activity
H248A
29.5%drop in protochlorophyllide a-oxygenase activity in the generated mutant proteins relative to the wild-type activity
H248A/H253A
88% drop in protochlorophyllide a-oxygenase activity in the generated mutant proteins relative to the wild-type activity
H253A
41.5% drop in protochlorophyllide a-oxygenase activity in the generated mutant proteins relative to the wild-type activity
H386A
0% drop in protochlorophyllide a-oxygenase activity in the generated mutant proteins relative to the wild-type activity
L440A
0% drop in protochlorophyllide a-oxygenase activityy in the generated mutant proteins relative to the wild-type activity
N399A
0% drop in protochlorophyllide a-oxygenase activity in the generated mutant proteins relative to the wild-type activity
P354A
94.5% drop in protochlorophyllide a-oxygenase activity in the generated mutant proteins relative to the wild-type activity
P441A
19% drop in protochlorophyllide a-oxygenase activity in the generated mutant proteins relative to the wild-type activity
R390A
0.5% drop in protochlorophyllide a-oxygenase activity in the generated mutant proteins relative to the wild-type activity
V249A
7.0% drop in protochlorophyllide a-oxygenase activity in the generated mutant proteins relative to the wild-type activity
W351A
15.5% drop in protochlorophyllide a-oxygenase activity in the generated mutant proteins relative to the wild-type activity
W400A
0.75% drop in protochlorophyllide a-oxygenase activity in the generated mutant proteins relative to the wild-type activity
A376V
the mutant shows reduced activity compared to the wild type enzyme
A94T
the mutant shows reduced activity compared to the wild type enzyme
C320Y
the mutant shows reduced activity compared to the wild type enzyme
L373F
the mutant shows reduced activity compared to the wild type enzyme
P419L
the mutant shows reduced activity compared to the wild type enzyme
additional information
A247D
25.0% drop in protochlorophyllide a-oxygenase activity in the generated mutant proteins relative to the wild-type activity
A247D
31.2% drop in protochlorophyllide a-oxygenase activity in the generated mutant proteins relative to the wild-type activity
additional information
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construction of domain mutants by combinating the three domains A, B, and C for construction of transgenic plants expressing the wild-type enzyme or domain A, or B, or C or a combinantion thereof, domain structure, transgenic subcellular localization, regulatory effects on chlorophyll a/b ratio and protein accumulation, overview
additional information
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construction of transgenic plants expressing the enzyme of Prochlirothrix hollandica in thylakoid membranes under control of the 35S CaMV promoter using the Agrobacterium tumefaciens infection system, the transgenic plants are capable of normal rate photosynthetic growth also under low light conditions in contrast to the wild-type plants, transgenic plants show an altered chlorophyll a/b ratio in photosystems I and II, chloroplast structure, and thylakoid membrane composition, phenotype, overview
additional information
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construction of transgenic plants functionally overexpressing the enzyme under control of the 35S CaMV promoter leading to 10-20% enlarged antenna size of photosystem II
additional information
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construction of transgenic tobacco plants overexpressing the enzyme, the transgenic plants show 72% increased CAO activity and light-dependent regulation of chlorophyll b biosynthesis
additional information
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enzyme level and activity is reduced in the conditional chlorina 1 mutant cch1
additional information
isolation of 3 mutant plants with increased enzyme mRNA levels but reduced chlorophyll b levels
additional information
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isolation of 3 mutant plants with increased enzyme mRNA levels but reduced chlorophyll b levels
additional information
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transgenic enzyme-overexpressing plants show accumulation of light-harvesting complexes and reduced beta-carotene levels compared to wild-type plants, while it is increased in enzyme-deficient chlorina-1 mutant plants, in overexpressing plants the chlorophyll a/b ratio remains low under high-light conditions in contrast to wild-type plants
additional information
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construction of homozygous loss-of-function mutants. Mutants contain a normally structured prolamellar body that contains the protochlorophyllide holochrome. Etioplasts from mutants contain protochlorophyllide oxidoreductase A protein
additional information
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construcution of a series of deleted enzyme sequences fused with green fluorescent protein and overexpressed in a chlorophyll b-less mutant. No significant difference in enzyme protein levels in transgenic plants overexpressing B domain containing proteins or those lacking the B domain
additional information
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transgenic plants overexpressing the N-terminal A domain accumulate an excess amount of chlorophyll b during greening. The plants either die or are obviously retarded when they are exposed to continuous light immediatley after etiolation. Loss of the A domain additionally impairs the conversion of divinyl protochlorophyllide a to monovinyl protochlorophyllide a under dark conditions
additional information
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seeds overexpressing A+B-domain-green fluorescent protein (AB-GFP) fusion enzyme, mutagenized by ethyl methane sulfonate overnight, 30000 lines of mutagenized transgenic plants screened for GFP fluorescence (excitation at 488 nm, emission at 522 nm) and observation of autofluorescence of chlorophyll (680 nm), 66 mutants with GFP signal isolated and grouped into 7 groups that are defined by the distribution pattern of the GFP signal, and characterized by pigment and immunoblotting analysis
additional information
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serial deletions in the A-domain identify the amino acid sequence Q97-DLLTIMIL-H106 that is essential for the regulation of the protein stability, this sequence introduced into mutant chlorina1-1 fusion enzyme lacking the entire A-domain re-enables the regulation of the enzyme, the other part of the A-domain is necessary to confer chlrorophyll-b dependency of the degradation process
additional information
construction of six chlorophyll-b less mutants by insertional mutagenesis, analysis of DNA rearrangements, overview
additional information
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construction of six chlorophyll-b less mutants by insertional mutagenesis, analysis of DNA rearrangements, overview
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additional information
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construction of transgenic tobacco plants overexpressing the Arabidopsis thaliana enzyme, the transgenic plants show 72% increased CAO activity and light-dependent regulation of chlorophyll b biosynthesis
additional information
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construction of CAO1 and CAO2 knockout mutants tagged by T-DNA or Tos-17, the CAO1 deficient mutant shows pale green leaves, the CAO2 deficient mutant show no altered leaf phenotype compared to the wild-type plants
additional information
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isolation of pale green rice mutants Y-15, a frame-shift mutant, and G-52, with a mutation of the lysine residue in the mononuclear iron-binding site, both mutant plants lack chlorophyll b, the pseudogene CAO-11 mutant shows no pale green leaf phenotype but a defect in the Rieske cluster
additional information
generation of the truncated enzyme mutant OsCAO1pgl. The premature translational termination of OsCAO1 in mutant pgl does not affect OsCAO1 localization, the mutation nevertheless results in the pale-green phenotype. Expression levels of Chl synthesis-associated genes in mutant pgl, and phenotype, overview
additional information
ZmCAO1 gene disruption by 51 bp pPopin transposon insertion abolishing transcription. Reduced enzyme activity of ZmCAO1 leads to reduced concentrations of chlorophyll a and chlorophyll b, resulting in the yellow-green leaf phenotype of the ygl mutant. The net photosynthetic rate, stomatal conductance, and transpiration rate are decreased in the ygl mutant, while concentrations of delta-aminolevulinic acid (ALA), porphobilinogen (PBG) and protochlorophyllide (Pchlide) are increased. In addition, a ZmCAO1 mutation results in downregulation of key photosynthetic genes, limits photosynthetic assimilation, and reduces plant height, ear size, kernel weight, and grain yield. Furthermore, the zmcao1 mutant shows enhanced reactive oxygen species production leading to sensitivity to waterlogging. These results demonstrate the pleiotropy of ZmCAO1 function in photosynthesis, grain yield, and waterlogging tolerance in maize. Phenotypes of the ygl and cao1cao1 mutants, detailed overview
additional information
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ZmCAO1 gene disruption by 51 bp pPopin transposon insertion abolishing transcription. Reduced enzyme activity of ZmCAO1 leads to reduced concentrations of chlorophyll a and chlorophyll b, resulting in the yellow-green leaf phenotype of the ygl mutant. The net photosynthetic rate, stomatal conductance, and transpiration rate are decreased in the ygl mutant, while concentrations of delta-aminolevulinic acid (ALA), porphobilinogen (PBG) and protochlorophyllide (Pchlide) are increased. In addition, a ZmCAO1 mutation results in downregulation of key photosynthetic genes, limits photosynthetic assimilation, and reduces plant height, ear size, kernel weight, and grain yield. Furthermore, the zmcao1 mutant shows enhanced reactive oxygen species production leading to sensitivity to waterlogging. These results demonstrate the pleiotropy of ZmCAO1 function in photosynthesis, grain yield, and waterlogging tolerance in maize. Phenotypes of the ygl and cao1cao1 mutants, detailed overview
